Watford M, Tatro A V
Division of Nutritional Sciences, Cornell University, Itaca, NY 14853.
J Nutr. 1989 Feb;119(2):268-72. doi: 10.1093/jn/119.2.268.
Phosphoenolpyruvate carboxykinase (PEPCK) activity is present along the length of rat small intestine and in enterocytes throughout the villus-crypt axis. There is no detectable activity in submucosal layers. Messenger RNA encoding PEPCK is detectable in rat intestinal mucosa and the relative abundance increases markedly (3- to 8-fold) during starvation or streptozotocin-diabetes. However, these changes are not matched by changes in enzyme activity which are only slightly increased (1.5-fold). The intestine of neonatal rats possesses relatively high amounts of both PEPCK activity and mRNA. Based on the distribution and regulation of intestinal PEPCK, it is proposed that the enzyme does not play a significant role in either gluconeogenesis or glutamine catabolism in adult rats.
磷酸烯醇式丙酮酸羧激酶(PEPCK)活性存在于大鼠小肠全长以及整个绒毛 - 隐窝轴的肠上皮细胞中。黏膜下层未检测到活性。编码PEPCK的信使核糖核酸在大鼠肠黏膜中可检测到,并且在饥饿或链脲佐菌素诱导的糖尿病期间相对丰度显著增加(3至8倍)。然而,这些变化与酶活性的变化并不匹配,酶活性仅略有增加(1.5倍)。新生大鼠的小肠具有相对较高水平的PEPCK活性和信使核糖核酸。基于肠道PEPCK的分布和调节,有人提出该酶在成年大鼠的糖异生或谷氨酰胺分解代谢中均不发挥重要作用。